ArticleThe Journal of biological chemistry2013
Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 78 citations in OpenAlex.
- Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Viruses · 2026Article
- Local Stress in Cylindrically Curved Lipid Membrane: Insights into Local Versus Global Lateral Fluidity Models.Biomolecules · 2024Article
- Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes.Nature communications · 2024Article
- Impacts of Hydrophobic Mismatch on Antimicrobial Peptide Efficacy and Bilayer Permeabilization.Antibiotics (Basel, Switzerland) · 2023Article
- Assembly of Cell-Free Synthesized Ion Channel Molecules in Artificial Lipid Bilayer Observed by Atomic Force Microscopy.Membranes · 2023Article
- Molecular substructure of the liquid-ordered phase formed by sphingomyelin and cholesterol: sphingomyelin clusters forming nano-subdomains are a characteristic feature.Biophysical reviews · 2022Article
- Self-organization of apical membrane protein sorting in epithelial cells.The FEBS journal · 2022Article
- Review
- Preparation and utility of asymmetric lipid vesicles for studies of perfringolysin O-lipid interactions.Methods in enzymology · 2021Article
- Preferential Protein Partitioning in Biological Membrane with Coexisting Liquid Ordered and Liquid Disordered Phase Behavior: Underlying Design Principles.The Journal of membrane biology · 2020Review
- The desmosome as a model for lipid raft driven membrane domain organization.Biochimica et biophysica acta. Biomembranes · 2020Review
- Peripheral myelin protein 22 preferentially partitions into ordered phase membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes.Chembiochem : a European journal of chemical biology · 2020Article
- Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting.Scientific reports · 2020Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- The Effect of Transmembrane Protein Shape on Surrounding Lipid Domain Formation by Wetting.Biomolecules · 2019Article
- Helicobacter pylori lipids can form ordered membrane domains (rafts).Biochimica et biophysica acta. Biomembranes · 2019Article
- Structural determinants and functional consequences of protein affinity for membrane rafts.Nature communications · 2017Article
- Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains.eLife · 2017Article
- Phase Composition Control in Microsphere-Supported Biomembrane Systems.Langmuir : the ACS journal of surfaces and colloids · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hypothesis that mismatch between transmembrane (TM) length and bilayer width controls TM protein affinity for ordered lipid domains (rafts) was tested using perfringolysin O (PFO), a pore-forming cholesterol-dependent cytolysin. PFO forms a multimeric barrel with many TM segments. The properties of PFO mutants with lengthened or shortened TM segments were compared with that of PFO with wild type TM sequences. Both mutant and wild type length PFO exhibited cholesterol-dependent membrane insertion. Maximal PFO-induced pore formation occurred in vesicles with wider bilayers for lengthened TM segments and in thinner bilayers for shortened TM segments. In diC(18:0) phosphatidylcholine (PC)/diC(14:1) PC/cholesterol vesicles, which form ordered domains with a relatively thick bilayer and disordered domains with a relatively thin bilayer, affinity for ordered domains was greatest with lengthened TM segments and least with shortened TM segments as judged by FRET. Similar results were observed by microscopy in giant vesicles containing sphingomyelin in place of diC(18:0) PC. In contrast, in diC(16:0) PC/diC(14:0) PC/diC(20:1) PC/cholesterol vesicles, which should form ordered domains with a relatively thin bilayer and disordered domains with a relatively thick bilayer, relative affinity for ordered domains was greatest with shortened TM segments and least with lengthened TM segments. The inability of multi-TM segment proteins (unlike single TM segment proteins) to adapt to mismatch by tilting may explain the sensitivity of raft affinity to mismatch. The difference in width sensitivity for single and multi-TM helix proteins may link raft affinity to multimeric state and thus control the assembly of multimeric TM complexes in rafts.
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